Collagenases

Collagen [9007-34-5] Collagen [9059-25-0] Collagenase [9001-12-1] Collective marks CoUectorless flotation Collector reagents Collectors... 

MMP-1 Interstitial collagenase Secreted One of three collagenases that can degrade the interstitial collagens, types I, II, and III... 

MMP-18 Collagenase 4, xcol4, xenopus collagenase — No known human orthologue... 

MA M9 M09.001 Bacterial collagenase (Vibrio-type) Potential agent for burn debridment... 

A topical enzyme aids in the removal of dead soft tissues by hastening the reduction of proteins into simpler substances. This is called proteolysis or a proteolytic action. The components of certain types of wounds, namely necrotic (dead) tissues and purulent exudates (pus-containing fluid), prevent proper wound healing. Removal of this type of debris by application of a topical enzyme aids in healing. Examples of conditions that may respond to application of a topical enzyme include second- and third-degree bums, pressure ulcers, and ulcers caused by peripheral vascular disease An example of a topical enzyme is collagenase (Santyl). 

The application of collagenase may cause mild, transient pain. Numbness and dennatitis also may be seen. Collagenase has a low incidence of adverse reactions. 

Collagenases and hyaluronidases are produced by most of the aggressive invaders. These are able to dissolve eollagen fibres and hyaluronie aeids which function as intracellular cements. Their loss causes the tissues to breakup and produce oedematous lesions. 

Collagenase is also produced by Cl. perfringens and this degrades collagen, which is the major protein offibrous tissue. Its destruction promotes the spread of infection in tissues. 

The PL-catechin conjugate showed greatly amplified concentration-dependent inhibition activity against bacterial collagenase (ChC) on the basis of the catechin unit, which is considered to be due to effective multivalent interaction between ChC and the catechin unit in the conjugate. The kinetic study suggests that this conjugate is a mixed-type inhibitor for ChC. Hyaluronidase is an enzyme which catalyzes hydrolysis of hyaluronic acid and is often involved in a number... 

Weiss, S.J., Peppin, G., Ortiz, X., Ragsdale, C. and Test, S.T. (1985). Oxidative autoactivation of latent collagenase by human neutrophils. Science 227, 747-749. 

The matrix metalloendoproteinases (MMPs or matrixins) are a family of zinc and calcium dependent extracellular proteases that collectively degrade most of the protein constituents of the extracellular matrix [9]. There are at least 23 members of this family and are divided primarily on the basis of sequence homology and substrate specificity into the following grouping collagenases (MMP-1, -8, -13, -18) gelatinases... 

Figure 2 Domain structure of the MMPs 92 kDa gelatinase-A (MMP-2), 72 kDa gelatinase-B (MMP-9), the collagenases (MMP-1, -8, and -13), stromelysin-1 (MMP-3) and matrilysin (MMP-7). Matrilysin is the only known MMP that does not have a C-terminal hemopexin-like domain.

An advantage of NMR spectroscopy is the analysis of protein dynamics. Measurement and analysis of the relaxation parameters R1 R2, and the 15N NOE of 15N-labeled proteins leads to an order parameter (S2) that can describe the relative mobility of the backbone of the protein. Both collagenase-1 and stromelysin-1 have been studied either as inhibited complexes or the free protein [19, 52], Stromleysin-1 was studied with inhibitors binding to prime or nonprime subsites. Presence or absence of inhibitors in the nonprime sites had minor effects on the highly ordered structure of residues in these subsites, which are in contact with the... 

Figure 12 Catalytic mechanism of thermolysin and stromelysin-1. (A) The mechanism of thermolysin [54], (B) The mechanism of stromleysin-1 [10]. Equivalent residues to Tyr-157 and His-231 are not observed for stromelysin-1. The proposed mechanism for collagenase-1 [S3] is similar to stromelysin-1, but also involves Asn-180 (equivalent to Asn-162 in stromelysin-1). This residue cannot participate in stromelysin-1 due to an additional residue between Ala-165 and Asn-162. (Adapted from Ref. 10.)...

Li J, Brick P, O Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE, Blow DM. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed (i-propellor. Structure 1995 3 541-549. 

Gomis-Ruth FX, Gohlke U, Betz M, Knauper Y, Murphy G, Lopez-Otin C, Bode W. The helping hand of collagenase-3 (MMP-13) 2.7 A crystal structure of its C-terminal haemopexin-like domain. J Mol Biol 1996 264 556-566. 

Bode W. A helping hand for collagenases the hemopexin-like domain. Structure 1995 3 527-530. 

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